Structure of PDB 1m7a Chain B

Receptor sequence
>1m7aB (length=192) Species: 5476 (Candida albicans) [Search protein sequence]
MLKPNVAIIVAALKPALGIGYKGKMPWRLRKEIRYFKDVTTRTTKPNTRN
AVIMGRKTWESIPQKFRPLPDRLNIILSRSYENEIIDDNIIHASSIESSL
NLVSDVERVFIIGGAEIYNELINNSLVSHLLITEIEHPSPESIEMDTFLK
FPLESWTKQPKSELQKFVGDTVLEDDIKEGDFTYNYTLWTRK
3D structure
PDB1m7a X-Ray Crystallographic Studies of Candida Albicans Dihydrofolate Reductase. High Resolution Structures of the Holoenzyme and an Inhibited Ternary Complex.
ChainB
Resolution1.76 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) M25 W27 E32 I33 F36 L69 V109 T133
Catalytic site (residue number reindexed from 1) M25 W27 E32 I33 F36 L69 V109 T133
Enzyme Commision number 1.5.1.3: dihydrofolate reductase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NDP B V10 A11 I19 G23 K24 M25 G55 R56 K57 T58 L77 S78 R79 I96 I112 G114 A115 E116 I117 E120 V10 A11 I19 G23 K24 M25 G55 R56 K57 T58 L77 S78 R79 I96 I112 G114 A115 E116 I117 E120
BS02 MQU B I9 V10 E32 F36 I112 I9 V10 E32 F36 I112 MOAD: ic50=9nM
Gene Ontology
Molecular Function
GO:0004146 dihydrofolate reductase activity
GO:0016491 oxidoreductase activity
GO:0050661 NADP binding
Biological Process
GO:0006730 one-carbon metabolic process
GO:0046452 dihydrofolate metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046655 folic acid metabolic process
Cellular Component
GO:0005739 mitochondrion

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Cellular Component
External links
PDB RCSB:1m7a, PDBe:1m7a, PDBj:1m7a
PDBsum1m7a
PubMed9374515
UniProtP22906|DYR_CANAX Dihydrofolate reductase (Gene Name=DFR1)

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